RL3_BRUA2
ID RL3_BRUA2 Reviewed; 237 AA.
AC Q2YM03;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325};
GN Name=rplC {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=BAB1_1255;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds directly
CC near the 3'-end of the 23S rRNA, where it nucleates assembly of the 50S
CC subunit. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with
CC proteins L14 and L19. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- PTM: Methylated by PrmB. {ECO:0000255|HAMAP-Rule:MF_01325}.
CC -!- SIMILARITY: Belongs to the universal ribosomal protein uL3 family.
CC {ECO:0000255|HAMAP-Rule:MF_01325}.
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DR EMBL; AM040264; CAJ11211.1; -; Genomic_DNA.
DR RefSeq; WP_002964362.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YM03; -.
DR SMR; Q2YM03; -.
DR STRING; 359391.BAB1_1255; -.
DR EnsemblBacteria; CAJ11211; CAJ11211; BAB1_1255.
DR GeneID; 3787853; -.
DR KEGG; bmf:BAB1_1255; -.
DR PATRIC; fig|359391.11.peg.155; -.
DR HOGENOM; CLU_044142_2_0_5; -.
DR OMA; KRMAGRY; -.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW.
DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR HAMAP; MF_01325_B; Ribosomal_L3_B; 1.
DR InterPro; IPR000597; Ribosomal_L3.
DR InterPro; IPR019927; Ribosomal_L3_bac/org-type.
DR InterPro; IPR019926; Ribosomal_L3_CS.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR PANTHER; PTHR11229; PTHR11229; 1.
DR Pfam; PF00297; Ribosomal_L3; 1.
DR SUPFAM; SSF50447; SSF50447; 1.
DR TIGRFAMs; TIGR03625; L3_bact; 1.
DR PROSITE; PS00474; RIBOSOMAL_L3; 1.
PE 3: Inferred from homology;
KW Methylation; Reference proteome; Ribonucleoprotein; Ribosomal protein;
KW RNA-binding; rRNA-binding.
FT CHAIN 1..237
FT /note="50S ribosomal protein L3"
FT /id="PRO_0000241324"
FT REGION 133..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 213..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 133..150
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01325"
SQ SEQUENCE 237 AA; 25064 MW; C89617EBC6E50AE5 CRC64;
MRSGVIAQKL GMTRVYNDAG EHVPVTVLRM ENCHVVAQRT VEKNGYTAVQ LGVGMAKVKN
TSKAMRGHFA KAEVEPKAKL AEFRVSPDNL LEVGVEITAE HFVAGQKVDV TGTSIGKGFA
GVMKRHNFGG HRASHGNSIT HRSHGSTGQR QDPGKVFKGK KMAGHMGQTR VTTQNIEVVS
TDSDRGLILV RGAVPGSKGA WILVRDAVKA SLPENAPKPA GLRAGAKAEA AATEGGE